ID A0A0B5DFF9_9ACTN Unreviewed; 209 AA.
AC A0A0B5DFF9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN ORFNames=BJY54_003815 {ECO:0000313|EMBL:MBB4793203.1}, CP978_19760
GN {ECO:0000313|EMBL:QEV40485.1}, SNOD_19435
GN {ECO:0000313|EMBL:AJE41959.1};
OS Streptomyces nodosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE41959.1, ECO:0000313|Proteomes:UP000031526};
RN [1] {ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT "Sequence of the Streptomyces nodosus genome.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJE41959.1, ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE41959.1,
RC ECO:0000313|Proteomes:UP000031526};
RX PubMed=26497174;
RA Sweeney P., Murphy C.D., Caffrey P.;
RT "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT antibiotic production.";
RL Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN [3] {ECO:0000313|EMBL:QEV40485.1, ECO:0000313|Proteomes:UP000325763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV40485.1,
RC ECO:0000313|Proteomes:UP000325763};
RA Lee N., Cho B.-K.;
RT "Streptomyces genome completion.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:MBB4793203.1, ECO:0000313|Proteomes:UP000544950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4793203.1,
RC ECO:0000313|Proteomes:UP000544950};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient.
CC {ECO:0000256|RuleBase:RU004429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={ECO:0000256|RuleBase:RU004429};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU004429};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU004429}.
CC -!- SIMILARITY: Belongs to the complex I subunit 6 family.
CC {ECO:0000256|ARBA:ARBA00005698, ECO:0000256|RuleBase:RU004429}.
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DR EMBL; CP009313; AJE41959.1; -; Genomic_DNA.
DR EMBL; JACHMR010000001; MBB4793203.1; -; Genomic_DNA.
DR EMBL; CP023747; QEV40485.1; -; Genomic_DNA.
DR RefSeq; WP_043442935.1; NZ_JACHMR010000001.1.
DR STRING; 40318.SNOD_19435; -.
DR KEGG; snq:CP978_19760; -.
DR HOGENOM; CLU_085957_2_0_11; -.
DR OrthoDB; 5244096at2; -.
DR Proteomes; UP000031526; Chromosome.
DR Proteomes; UP000325763; Chromosome.
DR Proteomes; UP000544950; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.1200; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1.
DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR PANTHER; PTHR33269:SF20; NADH-QUINONE OXIDOREDUCTASE SUBUNIT J; 1.
DR PANTHER; PTHR33269; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6; 1.
DR Pfam; PF00499; Oxidored_q3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU004429};
KW Membrane {ECO:0000256|RuleBase:RU004429};
KW NAD {ECO:0000256|RuleBase:RU004429};
KW Quinone {ECO:0000256|RuleBase:RU004429};
KW Reference proteome {ECO:0000313|Proteomes:UP000031526};
KW Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429}.
FT TRANSMEM 27..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 51..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 75..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 114..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 160..181
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT REGION 187..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 21677 MW; 1C70907215984699 CRC64;
MSPALAVAAT AVTGTHGFLS PTGVEIAFLL VGLVTFGAAL VTVTTRQLVH AALWLVVTLG
GLAVEYLLLT AEFIAWMQVL IYVGSVVVLL LFGLMLTKAP IGRSPDADSG NRPAALTVAV
AAGAALVWVV VDAFRTTWID LSGPASGSTE VTGASLFQHW VLPFEALSVL LLTALVGAIV
LSRRAKADEA TTESTPARPD ARSEKEGAR
//
